This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ouw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:50, 17 April 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ouw.gif|left|200px]]
 
-
{{Structure
+
==Crystal structure of Calystegia sepium agglutinin==
-
|PDB= 1ouw |SIZE=350|CAPTION= <scene name='initialview01'>1ouw</scene>, resolution 1.37&Aring;
+
<StructureSection load='1ouw' size='340' side='right'caption='[[1ouw]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MLT:MALATE+ION'>MLT</scene>
+
<table><tr><td colspan='2'>[[1ouw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Calystegia_sepium Calystegia sepium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OUW FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYA:N-ACETYLALANINE'>AYA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ouw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouw OCA], [https://pdbe.org/1ouw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ouw RCSB], [https://www.ebi.ac.uk/pdbsum/1ouw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ouw ProSAT]</span></td></tr>
-
|RELATEDENTRY=[[1c3k|1C3K]], [[1c3m|1C3M]], [[1c3n|1C3N]]
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ouw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ouw OCA], [http://www.ebi.ac.uk/pdbsum/1ouw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ouw RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/LECC_CALSE LECC_CALSE] Mannose-binding lectin (PubMed:9111143, PubMed:18266762, PubMed:14561768, PubMed:26971576, PubMed:28973127). Preferentially binds mannose at concentrations ranging between 5 and 25 mM, but binds also glucose. Has a marked preference for methylated sugar derivatives, such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM (PubMed:14561768). Binds to N-glycans, but not to glycolipid-type or other type of glycans (PubMed:28973127). Binds N-linked high-mannose-type glycans (PubMed:18266762, PubMed:28973127). Has a preference for smaller (Man(2)-Man(6)) high-mannose-type glycans to larger (Man(7)-Man(9)) ones. Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch results in a significant loss of affinity, but beta1-2GlcNAc has some affinity. Has less affinity for biantennary glycans (PubMed:18266762). However, affinity is significant for the biantennary complex-type N-glycans with bisecting GlcNAc (PubMed:18266762, PubMed:26971576, PubMed:28973127). No affinity is observed for tri- and tetra-antennary glycans (PubMed:18266762). Binds bisected glycans of the mouse brain. Selectively binds to bisecting N-glycans which are in back-fold conformation, and does not favor a glycan with an extend conformation (PubMed:26971576). Has hemagglutinating activity against rabbit erythrocytes at 0.3 ug/ml and against trypsin-treated human erythrocytes at 5 ug/ml. Has mitogenic activity in murine cells (PubMed:9111143).<ref>PMID:14561768</ref> <ref>PMID:18266762</ref> <ref>PMID:26971576</ref> <ref>PMID:28973127</ref> <ref>PMID:9111143</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/1ouw_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ouw ConSurf].
 +
<div style="clear:both"></div>
-
'''Crystal structure of Calystegia sepium agglutinin'''
+
==See Also==
-
 
+
*[[Agglutinin 3D structures|Agglutinin 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
The high number of quaternary structures observed for lectins highlights the important role of these oligomeric assemblies during carbohydrate recognition events. Although a large diversity in the mode of association of lectin subunits is frequently observed, the oligomeric assemblies of plant lectins display small variations within a single family. The crystal structure of the mannose-binding jacalin-related lectin from Calystegia sepium (Calsepa) has been determined at 1.37-A resolution. Calsepa exhibits the same beta-prism fold as identified previously for other members of the family, but the shape and the hydrophobic character of its carbohydrate-binding site is unlike that of other members, consistent with surface plasmon resonance analysis showing a preference for methylated sugars. Calsepa reveals a novel dimeric assembly markedly dissimilar to those described earlier for Heltuba and jacalin but mimics the canonical 12-stranded beta-sandwich dimer found in legume lectins. The present structure exemplifies the adaptability of the beta-prism building block in the evolution of plant lectins and highlights the biological role of these quaternary structures for carbohydrate recognition.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1OUW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Calystegia_sepium Calystegia sepium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OUW OCA].
+
-
 
+
-
==Reference==
+
-
The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold., Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rouge P, J Biol Chem. 2004 Jan 2;279(1):527-33. Epub 2003 Oct 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14561768 14561768]
+
[[Category: Calystegia sepium]]
[[Category: Calystegia sepium]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Astoul, C H.]]
+
[[Category: Astoul CH]]
-
[[Category: Barre, A.]]
+
[[Category: Barre A]]
-
[[Category: Bourne, Y.]]
+
[[Category: Bourne Y]]
-
[[Category: Damme, E J.M van.]]
+
[[Category: Peumans WJ]]
-
[[Category: Peumans, W J.]]
+
[[Category: Roig-Zamboni V]]
-
[[Category: Roig-Zamboni, V.]]
+
[[Category: Rouge P]]
-
[[Category: Rouge, P.]]
+
[[Category: Van Damme EJM]]
-
[[Category: agglutinin]]
+
-
[[Category: beta-prism fold]]
+
-
[[Category: jacalin-related]]
+
-
[[Category: lectin]]
+
-
[[Category: mannose-binding]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:50:40 2008''
+

Current revision

Crystal structure of Calystegia sepium agglutinin

PDB ID 1ouw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ouw"
Personal tools